5YR7
Human methionine aminopeptidase type 1b (F309L mutant)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2017-03-19 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 47.414, 77.193, 48.220 |
Unit cell angles | 90.00, 92.03, 90.00 |
Refinement procedure
Resolution | 23.690 - 2.060 |
R-factor | 0.1991 |
Rwork | 0.196 |
R-free | 0.26620 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2b3k |
RMSD bond length | 0.015 |
RMSD bond angle | 1.699 |
Data reduction software | DENZO (2.3.1) |
Data scaling software | SCALEPACK (2.2.0) |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 25.000 | 25.000 | 2.130 |
High resolution limit [Å] | 2.060 | 4.430 | 2.060 |
Rmerge | 0.068 | 0.040 | 0.450 |
Rmeas | 0.088 | 0.051 | 0.586 |
Rpim | 0.055 | 0.032 | 0.371 |
Number of reflections | 17388 | 1806 | 1684 |
<I/σ(I)> | 12.8 | ||
Completeness [%] | 79.9 | 81.1 | 78.1 |
Redundancy | 2 | 2.1 | 1.9 |
CC(1/2) | 0.994 | 0.780 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.2 | 298 | 0.1M Bistris pH-6.2, 19% PEG 3350, 5% Glycerol |